Contribution of the plasmin/matrix metalloproteinase cascade to the retraction of human fibroblast populated collagen lattices. - Archive ouverte HAL Access content directly
Journal Articles Molecular Cell Biology Research Communications Year : 2000

Contribution of the plasmin/matrix metalloproteinase cascade to the retraction of human fibroblast populated collagen lattices.

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Abstract

To assess the contribution of the plasmin/matrix metalloproteinase cascade in lattices retraction, human gingival fibroblast-populated collagen lattices were supplemented with plasminogen. The rate of lattice retraction was enhanced by addition of plasminogen. This effect was concomitant to plasmin generation, prostromelysin-1 and procollagenase activation. Plasminogen-mediated initiation of that proteolytic cascade was accompanied by conspicuous changes in cell morphology and collagen fibers organization. At day 1 of culture fibroblasts shifted from a rounded (control) to an elongated (in presence of plgn) shape. At the latest stage of retraction, intense vacuolization around fibroblasts was noticed in plgn-supplemented lattices which paralleled the increased collagen degradation. Plgn-enhancing influence on the initial phase of lattice retraction could be totally annihilated by either aprotinin or Batimastat. Those data emphasize the crucial importance of the plasmin-MMP proteolytic cascade in granulation tissue retraction in a healing wound.

Dates and versions

inserm-00069571 , version 1 (18-05-2006)

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Alix Berton, Sandrine Lorimier, Hervé Emonard, Dominique Laurent-Maquin, William Hornebeck, et al.. Contribution of the plasmin/matrix metalloproteinase cascade to the retraction of human fibroblast populated collagen lattices.. Molecular Cell Biology Research Communications, 2000, 3, pp.173-80. ⟨10.1006/mcbr.2000.0210⟩. ⟨inserm-00069571⟩

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